KITH_ASFWA
ID KITH_ASFWA Reviewed; 196 AA.
AC P0C8I6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Thymidine kinase;
DE Short=TDK;
DE EC=2.7.1.21;
GN OrderedLocusNames=War-060;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates thymidine. ASFV replicates in the cytoplasm of
CC infected cells and contains genes encoding a number of enzymes needed
CC for DNA synthesis, including thymidine kinase. Important for growth in
CC swine macrophages in vitro and is a virus virulence factor in swine (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21;
CC -!- SIMILARITY: Belongs to the thymidine kinase family. {ECO:0000305}.
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DR EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C8I6; -.
DR Proteomes; UP000000858; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004797; F:thymidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001267; Thymidine_kinase.
DR InterPro; IPR020633; Thymidine_kinase_CS.
DR PANTHER; PTHR11441; PTHR11441; 1.
DR Pfam; PF00265; TK; 1.
DR PIRSF; PIRSF035805; TK_cell; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00603; TK_CELLULAR_TYPE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA synthesis; Kinase; Metal-binding; Nucleotide-binding;
KW Transferase; Virulence; Zinc.
FT CHAIN 1..196
FT /note="Thymidine kinase"
FT /id="PRO_0000355225"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 166..170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 22439 MW; DB1325CE2853C15C CRC64;
MNIIRKLKPG TISLVLGPMF AGKTTFLIHC IYMLEHLEKK VVFIKSTKNT RDKTIKTHSG
IQLRPKHCKI IESTQLSDVG SLTDIHAVVI DEAHFFDDLI KCRTWADEEK IIILAGLNAS
FEQKMFPPIV RIFPYCSWVK YIGRTCMKCN RHNACFNVRK NADKTLILAG GSELYVTCCN
NCLKNTFIKQ LQPIKY